Open AccessKinetic Studies of N ‐Allenic Analogues of Tryptamine as Monoamine Oxidase Inhibitors
Author(s) -
Perez V.,
Marco J. L.,
FernandezAlvarez E.,
Unzeta M.
Publication year - 1996
Publication title -
journal of pharmacy and pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 118
eISSN - 2042-7158
pISSN - 0022-3573
DOI - 10.1111/j.2042-7158.1996.tb03958.x
Subject(s) - tryptamine , chemistry , indole test , stereochemistry , monoamine oxidase , side chain , selectivity , potency , ring (chemistry) , enzyme , biochemistry , organic chemistry , in vitro , catalysis , polymer
A series of N ‐allenic analogues of tryptamine in which the side chain is located at the 2 position of the indole ring, but which differed in the ring and side‐chain nitrogen substituents, were assayed kinetically as MAO A and MAO B inhibitors. All the compounds studied were mechanism‐based inhibitors. The kinetic constants of each inhibition step K i and k i , were determined for both MAO A and B. The data obtained indicated that these allenic derivatives show a greater selectivity and potency towards MAO A as inhibitors than the corresponding acetylenic derivatives.